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http://purl.uniprot.org/citations/18675248http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18675248http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18675248http://www.w3.org/2000/01/rdf-schema#comment"Kf-1 was first identified as a gene showing enhanced expression in the cerebral cortex of a sporadic Alzheimer's disease patient. To date, however, the functional properties of Kf-1 protein remain unknown. In this study, immunohistochemical analysis showed that Kf-1 immunoreactivity was detected in rat hippocampus and cerebral cortex neurons. Interestingly, it was colocalized with endoplasmic reticulum (ER) marker. To investigate the specific function of Kf-1 protein, we generated Myc tagged wild type Kf-1 (Myc-Kf-1WT) and RING finger domain deletion mutant of Kf-1 (Myc-Kf-1DeltaR), and then transfected in HEK293 cells. Myc-Kf-1WT displayed a reticular pattern typical of ER localization, with large perinuclear aggregates and colocalized with ER marker, calnexin. Myc-Kf-1WT facilitated ubiquitination of endogenous proteins, whereas Myc-Kf-1DeltaR did not show ubiquitin ligase activity. In addition, we found that Kf-1 interacted with components of the ER-associated degradation (ERAD) pathway, including Derlin-1 and VCP. Taken together, these properties suggest that Kf-1 is an ER ubiquitin ligase involved in the ERAD pathway."xsd:string
http://purl.uniprot.org/citations/18675248http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2008.07.126"xsd:string
http://purl.uniprot.org/citations/18675248http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2008.07.126"xsd:string
http://purl.uniprot.org/citations/18675248http://purl.uniprot.org/core/author"Maruyama Y."xsd:string
http://purl.uniprot.org/citations/18675248http://purl.uniprot.org/core/author"Maruyama Y."xsd:string
http://purl.uniprot.org/citations/18675248http://purl.uniprot.org/core/author"Yamada M."xsd:string
http://purl.uniprot.org/citations/18675248http://purl.uniprot.org/core/author"Yamada M."xsd:string
http://purl.uniprot.org/citations/18675248http://purl.uniprot.org/core/author"Takahashi K."xsd:string
http://purl.uniprot.org/citations/18675248http://purl.uniprot.org/core/author"Takahashi K."xsd:string
http://purl.uniprot.org/citations/18675248http://purl.uniprot.org/core/author"Yamada M.'"xsd:string
http://purl.uniprot.org/citations/18675248http://purl.uniprot.org/core/author"Yamada M.'"xsd:string
http://purl.uniprot.org/citations/18675248http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18675248http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18675248http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/18675248http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/18675248http://purl.uniprot.org/core/pages"737-741"xsd:string
http://purl.uniprot.org/citations/18675248http://purl.uniprot.org/core/pages"737-741"xsd:string
http://purl.uniprot.org/citations/18675248http://purl.uniprot.org/core/title"Ubiquitin ligase Kf-1 is involved in the endoplasmic reticulum-associated degradation pathway."xsd:string
http://purl.uniprot.org/citations/18675248http://purl.uniprot.org/core/title"Ubiquitin ligase Kf-1 is involved in the endoplasmic reticulum-associated degradation pathway."xsd:string
http://purl.uniprot.org/citations/18675248http://purl.uniprot.org/core/volume"374"xsd:string
http://purl.uniprot.org/citations/18675248http://purl.uniprot.org/core/volume"374"xsd:string
http://purl.uniprot.org/citations/18675248http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18675248
http://purl.uniprot.org/citations/18675248http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18675248